RT null
T1 The C2 domains of classical/conventional PKCs are specific PtdIns(4,5)P(2)-sensing domains.
A1 Corbalán-García, Senena
A1 Marín-Vicente, Consuelo
A1 Gómez-Fernández, Juan Carmelo
A1 Guerrero Valero, Marta
AB The C2 domains of cPKCs [classical/conventional PKCs (protein kinase Cs)] bind to membranes in a Ca2+-dependent manner and thereby act as cellular Ca2+ effectors. Recent findings have demonstrated that the C2 domain of cPKCs interacts specifically with PtdIns(4,5)P2 through its polybasic cluster located in the β3–β4-strands, this interaction being critical for the membrane localization of these enzymes in living cells. In addition, these C2 domains exhibit higher affinity to bind PtdIns(4,5)P2 than any other polyphosphate phosphatidylinositols. It has also been shown that the presence of PtdIns(4,5)P2 in model membranes decreases the Ca2+ concentration required for classical C2 domains to bind them. Overall, the studies reviewed here suggest a new mechanism of membrane docking by the C2 domains of cPKCs in which the local densities of phosphatidylserine and PtdIns(4,5)P2 on the inner leaflet of the plasma membrane are sufficient to drive Ca2+-activated membrane docking during a physiological Ca2+ signal.
PB Portland Press Ltd
YR 2007
FD 2007
LK https://hdl.handle.net/20.500.14352/133150
UL https://hdl.handle.net/20.500.14352/133150
LA eng
NO Corbalán-García S, Guerrero-Valero M, Marín-Vicente C, et al. The C2 domains of classical/conventional PKCs are specific PtdIns(4,5) P 2-sensing domains. Biochemical Society Transactions 2007;35:1046–8. https://doi.org/10.1042/BST0351046
NO Fundación Ramón Areces (España)
NO Fundación Médica Mutua Madrileña (España)
NO Fundación Séneca (Región de Murcia, España)
NO Dirección General de Investigación (Comunidad de Madrid)
DS Docta Complutense
RD 19 mar 2026